Research workbench
AlphaFold monomer V2.0 prediction for phosphatidylethanolamine N-methyltransferase (C5FZ62)
Analyse AlphaFold monomer V2.0 prediction for phosphatidylethanolamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5FZ62
- Type
- protein
- Length
- 962 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC1C81C5d9568Be2795E0Bd2e795B6bD277CaDb67
- Molecule
- Phosphatidylethanolamine N-methyltransferase
- UniProt
- C5FZ62
- Pockets
- 13 · best druggability 0.78
Structure
1 distinct chain · 53% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylethanolamine N-methyltransferase | protein | 962 | 53% helix, 7% strand | C5FZ62 |
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 581 | 0.78 | 0.84 | 60 | empty |
| 2 | 693 | 0.76 | 0.81 | 76 | empty |
| 3 | 576 | 0.70 | 0.78 | 53 | empty |
| 4 | 315 | 0.70 | 0.83 | 36 | empty |
| 5 | 468 | 0.67 | 0.78 | 49 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt C5FZ62
- Elsewhere: UniProt C5FZ62 · AlphaFold DB C5FZ62
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